1zwu
From Proteopedia
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[[Image:1zwu.png|left|200px]] | [[Image:1zwu.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1zwu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWU OCA]. | |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:16220560</ref><ref group="xtra">PMID:8627629</ref><ref group="xtra">PMID:12144516</ref><ref group="xtra">PMID:15368576</ref><ref group="xtra">PMID:10842338</ref><ref group="xtra">PMID:10903932</ref><ref group="xtra">PMID:10877847</ref><references group="xtra"/> | |
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[[Category: Aboitiz, N.]] | [[Category: Aboitiz, N.]] | ||
[[Category: Andreu, C.]] | [[Category: Andreu, C.]] | ||
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[[Category: Alpha-helix]] | [[Category: Alpha-helix]] | ||
[[Category: Anti-parallel beta-sheet.]] | [[Category: Anti-parallel beta-sheet.]] | ||
| - | + | [[Category: Antimicrobial protein]] | |
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Revision as of 23:08, 14 March 2011
30 NMR structures of AcAMP2-like peptide with non natural beta-(2-naphthyl)-alanine residue.
Template:ABSTRACT PUBMED 16220560
About this Structure
1zwu is a 1 chain structure. Full experimental information is available from OCA.
Reference
- Chavez MI, Andreu C, Vidal P, Aboitiz N, Freire F, Groves P, Asensio JL, Asensio G, Muraki M, Canada FJ, Jimenez-Barbero J. On the importance of carbohydrate-aromatic interactions for the molecular recognition of oligosaccharides by proteins: NMR studies of the structure and binding affinity of AcAMP2-like peptides with non-natural naphthyl and fluoroaromatic residues. Chemistry. 2005 Nov 18;11(23):7060-74. PMID:16220560 doi:10.1002/chem.200500367
- Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33. PMID:8627629
- Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209. PMID:12144516
- Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55. PMID:15368576 doi:10.1002/cbic.200400025
- Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N"-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36. PMID:10842338
- Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43. PMID:10903932
- Muraki M, Morii H, Harata K. Chemically prepared hevein domains: effect of C-terminal truncation and the mutagenesis of aromatic residues on the affinity for chitin. Protein Eng. 2000 Jun;13(6):385-9. PMID:10877847
